Disease relevance of RRAS

• Our findings demonstrate that p23 differentially regulates ER target genes and is involved in the control of distinct cellular processes in breast tumor development, thus revealing novel functions of this cochaperone [1].

High impact information on RRAS

• To identify proteins that bind to the Ras-related protein R-ras we performed a yeast two-hybrid cDNA library screen [2].
• In this study, we investigated how p23 regulates ER target gene activation and affects tumor growth and progression [1].
• The cochaperone p23 differentially regulates estrogen receptor target genes and promotes tumor cell adhesion and invasion [1].
• The cochaperone p23 plays an important role in estrogen receptor alpha (ER) signal transduction [1].
• The N-terminal (N) domain of Hsp90 does not affect the NMR spectrum of p23 either in the presence or absence of the ATP analogue ATPgammaS [3].

Biological context of RRAS

• We have localized the SR-A1 gene between the known genes IRF3 and RRAS on chromosome 19q13 [4].
• Three simple sequence motifs were identified in and around the ERCC1 DNA-repair gene at 19q13.2-13.3 and one in the vicinity of the RRAS gene at 19q13.3-qter [5].
• The mouse cardiac p20 contains the conserved domain sequences for heat shock proteins, and the RRAS consensus sequence for cAMP-PKA substrates [6].

Associations of RRAS with chemical compounds

• The co-chaperone p23 forms a complex with the chaperone Hsp90 that mediates the folding pathway leading to the production of functional steroid receptors [3].

Other interactions of RRAS

• PRMT1, which spans 11.2 kb of genomic sequence on chromosome 19q13.3, is located in close proximity to the IRF3 and RRAS genes and is transcribed in the opposite direction [7].

Analytical, diagnostic and therapeutic context of RRAS

• Titration of p23 with Hsp90 results in the selective broadening of certain cross-peaks in the 15N-1H heteronuclear single quantum correlation (HSQC) spectrum [3].
• The interaction sites on p23 and Hsp90 have been localized by dissection of Hsp90 into single-domain and two-domain constructs [3].

References